ID C7N9C3_LEPBD Unreviewed; 419 AA. AC C7N9C3; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 27-MAR-2024, entry version 84. DE RecName: Full=Aspartokinase {ECO:0000256|RuleBase:RU003448}; DE EC=2.7.2.4 {ECO:0000256|RuleBase:RU003448}; GN OrderedLocusNames=Lebu_0846 {ECO:0000313|EMBL:ACV38754.1}; OS Leptotrichia buccalis (strain ATCC 14201 / DSM 1135 / JCM 12969 / OS NCTC 10249 / C-1013-b). OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Leptotrichiaceae; OC Leptotrichia. OX NCBI_TaxID=523794 {ECO:0000313|EMBL:ACV38754.1, ECO:0000313|Proteomes:UP000001910}; RN [1] {ECO:0000313|EMBL:ACV38754.1, ECO:0000313|Proteomes:UP000001910} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 14201 / DSM 1135 / JCM 12969 / NCTC 10249 / C-1013-b RC {ECO:0000313|Proteomes:UP000001910}; RX PubMed=21304648; DOI=10.4056/sigs.1854; RA Ivanova N., Gronow S., Lapidus A., Copeland A., Glavina Del Rio T., RA Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Saunders E., Bruce D., RA Goodwin L., Brettin T., Detter J.C., Han C., Pitluck S., Mikhailova N., RA Pati A., Mavrommatis K., Chen A., Palaniappan K., Land M., Hauser L., RA Chang Y.J., Jeffries C.D., Chain P., Rohde C., Goker M., Bristow J., RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of Leptotrichia buccalis type strain (C-1013- RT b)."; RL Stand. Genomic Sci. 1:126-132(2009). CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-aspartate = 4-phospho-L-aspartate + ADP; CC Xref=Rhea:RHEA:23776, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:57535, ChEBI:CHEBI:456216; EC=2.7.2.4; CC Evidence={ECO:0000256|ARBA:ARBA00000709, CC ECO:0000256|RuleBase:RU003448}; CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP CC pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 1/4. CC {ECO:0000256|ARBA:ARBA00004766, ECO:0000256|RuleBase:RU004249}. CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo CC pathway; L-homoserine from L-aspartate: step 1/3. CC {ECO:0000256|ARBA:ARBA00004986, ECO:0000256|RuleBase:RU004249}. CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine CC from L-aspartate: step 1/5. {ECO:0000256|ARBA:ARBA00005139, CC ECO:0000256|RuleBase:RU004249}. CC -!- SIMILARITY: Belongs to the aspartokinase family. CC {ECO:0000256|ARBA:ARBA00010122, ECO:0000256|RuleBase:RU003448}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP001685; ACV38754.1; -; Genomic_DNA. DR RefSeq; WP_015769102.1; NC_013192.1. DR AlphaFoldDB; C7N9C3; -. DR STRING; 523794.Lebu_0846; -. DR KEGG; lba:Lebu_0846; -. DR eggNOG; COG0527; Bacteria. DR HOGENOM; CLU_009116_3_2_0; -. DR OrthoDB; 9799110at2; -. DR UniPathway; UPA00034; UER00015. DR UniPathway; UPA00050; UER00461. DR UniPathway; UPA00051; UER00462. DR Proteomes; UP000001910; Chromosome. DR GO; GO:0004072; F:aspartate kinase activity; IEA:UniProtKB-EC. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniPathway. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniPathway. DR CDD; cd04261; AAK_AKii-LysC-BS; 1. DR CDD; cd04923; ACT_AK-LysC-DapG-like_2; 1. DR CDD; cd04913; ACT_AKii-LysC-BS-like_1; 1. DR Gene3D; 3.40.1160.10; Acetylglutamate kinase-like; 1. DR Gene3D; 3.30.2130.10; VC0802-like; 1. DR InterPro; IPR036393; AceGlu_kinase-like_sf. DR InterPro; IPR045865; ACT-like_dom_sf. DR InterPro; IPR002912; ACT_dom. DR InterPro; IPR041740; AKii-LysC-BS. DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase. DR InterPro; IPR005260; Asp_kin_monofn. DR InterPro; IPR001341; Asp_kinase. DR InterPro; IPR018042; Aspartate_kinase_CS. DR InterPro; IPR027795; CASTOR_ACT_dom. DR InterPro; IPR001057; Glu/AcGlu_kinase. DR NCBIfam; TIGR00656; asp_kin_monofn; 1. DR NCBIfam; TIGR00657; asp_kinases; 1. DR PANTHER; PTHR21499; ASPARTATE KINASE; 1. DR PANTHER; PTHR21499:SF3; ASPARTOKINASE; 1. DR Pfam; PF00696; AA_kinase; 1. DR Pfam; PF01842; ACT; 1. DR Pfam; PF13840; ACT_7; 1. DR PIRSF; PIRSF000726; Asp_kin; 2. DR PRINTS; PR00474; GLU5KINASE. DR SUPFAM; SSF55021; ACT-like; 2. DR SUPFAM; SSF53633; Carbamate kinase-like; 1. DR PROSITE; PS51671; ACT; 1. DR PROSITE; PS00324; ASPARTOKINASE; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, KW ECO:0000256|RuleBase:RU004249}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR000726- KW 1}; Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU003448}; KW Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, KW ECO:0000256|PIRSR:PIRSR000726-1}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003448}. FT DOMAIN 278..362 FT /note="ACT" FT /evidence="ECO:0000259|PROSITE:PS51671" FT BINDING 7..10 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR000726-1" FT BINDING 47 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000726-1" FT BINDING 74 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000726-1" FT BINDING 173..174 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR000726-1" FT BINDING 179 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR000726-1" FT BINDING 184 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR000726-1" FT BINDING 209..210 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR000726-1" SQ SEQUENCE 419 AA; 45510 MW; 5F234D792EF5DF76 CRC64; MALIIQKYGG TSVANAERVK EVAKRVVKYK KAGHDVIVVV SAPAGRTDAL IKRAYELSDT PNKREFDMLL TSGEQISIAS LAIAVSELGE KAVSLNAFQV NFKTTSAHTK AKIIDIDTEL IQEKLNEGNV VVFAGFQGIT KNNEITTLGR GGSDTTAVAL GAALNADEVE IYTDVDGVYT ADPRVVKEAK KIKTISYQEM LELAASGAKV LHPRSVEIAA KYGIKIHLRS SFDDSTGTIV ENKKTIDEIE SQNINTKGDA MEKVKIVGIT SSKNEGRITL FGVPDRPGIA SKVFSRLAKS KINTDIILQS SSINKELNNI SFTVKSDDLK EAVAISEQIK EKIGAEGVSY EEKIAKVSVV GIGLKTHYET TSEIFDTLAE NNINIDMISC SEINVSCIIR EEDVDKAVNA LHKRFIEID //